Article
Elimination of N-glycosylation by site mutation further prolongs the half-life of IFN-α/Fc fusion proteins expressed in Pichia pastoris.
Microbial cell factories - 7 Dec 2016
Jia Hao, Guo Yugang, Song Xiaoping, Shao Changsheng, Wu Jing, Ma Jiajia, Shi Mingyang, Miao Yuhui, Li Rui, Wang Dong, Tian Zhigang, Xiao Weihua
Abstract excerpt
BACKGROUND: Interferon (IFN)-α has been commonly used as an antiviral drug worldwide; however, its short half-life in circulation due to its low molecular weight and sensitivity to proteases impacts its efficacy and patient compliance. RESULTS: In this study, we present an IgG1 Fc fusion strategy to improve the circulation half-life of IFN-α. Three different forms of IgG1 Fc fragments, including the wild type,...
Topics
- Animals
- Glycosylation
- Immunoglobulin Fc Fragments
- Interferon-alpha
- Mutation
- Pichia
- Rats
- Recombinant Fusion Proteins